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Abstract

A galactose-binding
lectin, isolated from the venom of B. gotlmani by affinity chromatography . is
an acidic protein (pI 4.9) with a subunit mol. wt of about 14,000, occurring
mostly as a disulfide-linked dimer of 28,000. A small proportion of lectin
appears as a monomer and as a tetramer. The lectin agglutinates erythrocytes
from mice, rabbit, cow and human (all ABO types, either Rh positive or
negative), but does not agglutinate horse, sheep, goat and snake (Oxybelis
aeneus, Colubridae) erythrocytes . The agglutinating activity is inhibited by
1 mM EDTA. The lectin is devoid of lethal, hemorrhagic, myotoxic, proteolytic
and phospholipase A2 activities . It is not mitogenic for human peripheral
blood mononuclear cells. The only effect observed was amoderate induction of
edema in the footpad of mice, with a minimal edema-forming dose of 22 kg.
This effect developed rapidly, and was significantly inhibited by i.p . administration
of cyproheptadine, a histamine and serotonin antagonist, before injection
of the lectin . Despite the edema-forming activity observed, the low
concentration of lectin in crude venom, together with its relatively low
potency, suggest that this lectin is not a key component in the development of
edema following envenomations by B. godrnani.